1. Facilitated antigen presentation and its inhibition by blocking IgG antibodies depends on IgE repertoire complexity 
Jens Holm, PhD, Nicholas Willumsen, MSc, Peter A. Würtzen, PhD, Lars H. Christensen, PhD, Kaare Lund, PhD 
Journal of Allergy and Clinical Immunology 
Volume 127, Issue 4, Pages (April 2011)
DOI: /j.jaci
Copyright © 2011 American Academy of Allergy, Asthma & Immunology Terms and Conditions

2. Fig 1
FACS assay. Similar levels of complex formation (percentage of B cells with bound IgE-allergen complexes) were obtained with 2 high-affinity rIgE antibody specificities (H10 plus P4E) on increasing amounts of rDer p 2 (solid circles) or D pteronyssinus extract (open circles) shown in the top and bottom x-axes, respectively. x-Axes were aligned according to the content of 85 ng of Der p 2 per microgram of protein in the extract.
Journal of Allergy and Clinical Immunology  , DOI: ( /j.jaci )
Copyright © 2011 American Academy of Allergy, Asthma & Immunology Terms and Conditions

3. Fig 2
A, FACS assay. Increase in antibody affinity or clonality affects complex formation positively. rIgE antibodies binding allergen with high affinity (h), medium affinity (m), or low affinity (l) were tested at increasing concentrations of D pteronyssinus extract. For details regarding IgE specificities, see Table I. Shown complex formation (percentage of B cells with bound IgE-allergen complexes) is normalized according to the maximum complex formation defined by 3 IgE antibody specificities (hhh; ie, data point: 3 μg/mL = 89.6% and was set to 100%). B and C, T-cell activation. FAP measured as B cell–mediated T-cell proliferation in cell lines 1 (Fig 2, B) and 2 (Fig 2, C) on varying rIgE affinity to Der p 2. Decreasing the affinity of rIgE antibodies for complex formation reduces the proliferative response by T cells.
Journal of Allergy and Clinical Immunology  , DOI: ( /j.jaci )
Copyright © 2011 American Academy of Allergy, Asthma & Immunology Terms and Conditions

4. Fig 3
FACS assay. Decreasing specific IgE concentration decreases complex formation. Graphs show complex formation measured as the percentage of B cells with bound IgE-allergen complexes with rDer p 2 in dilution series on testing 1:1:1 mixes of 3 rIgE antibody specificities. Undiluted samples (■; total [rIgE], 0.4 μg/mL) and samples diluted 2-fold (Δ), 4-fold (∇), and 8-fold (♢) are shown. A, B, and C: High-, medium-, or low-affinity IgE, respectively.
Journal of Allergy and Clinical Immunology  , DOI: ( /j.jaci )
Copyright © 2011 American Academy of Allergy, Asthma & Immunology Terms and Conditions

5. Fig 4
FACS assay. Complex formation obtained at a fixed concentration (0.4 μg/mL) of total IgE on changing the ratio between individual antibody specificities from 33% + 33% + (33%) to 0% + 0% + (100%). Complex formation was measured as the percentage of B cells with bound IgE-allergen complexes. rIgE specificity H10 is shown in brackets. A, B, and C, High-affinity (h), medium-affinity (m), or low-affinity (l) IgE, respectively.
Journal of Allergy and Clinical Immunology  , DOI: ( /j.jaci )
Copyright © 2011 American Academy of Allergy, Asthma & Immunology Terms and Conditions

6. Fig 5
FACS assay. A-C, Complex formation (percentage of B cells binding IgE-allergen complexes) obtained with 2 or 3 rIgEs inhibited by 2 or 3 specific rIgG antibodies, respectively, in titration. Pairwise, the rIgE and rIgG antibodies bind identical epitopes on Der p 2 with high affinity. For details regarding IgE specificities, see Table I. D, Complex formation with serum from a patient with mite allergy inhibited by 1 (H10), 2 (H10 + E), or 3 (H10 + H12 + E) specific rIgG antibody specificities.
Journal of Allergy and Clinical Immunology  , DOI: ( /j.jaci )
Copyright © 2011 American Academy of Allergy, Asthma & Immunology Terms and Conditions